1HLZ
CRYSTAL STRUCTURE OF THE ORPHAN NUCLEAR RECEPTOR REV-ERB(ALPHA) DNA-BINDING DOMAIN BOUND TO ITS COGNATE RESPONSE ELEMENT
1HLZ の概要
| エントリーDOI | 10.2210/pdb1hlz/pdb |
| 関連するPDBエントリー | 1A6Y 1GA5 |
| 分子名称 | 5'-D(*CP*AP*AP*CP*TP*AP*GP*GP*TP*CP*AP*CP*TP*AP*GP*GP*TP*CP*AP*G)-3', 5'-D(*CP*TP*GP*AP*CP*CP*TP*AP*GP*TP*GP*AP*CP*CP*TP*AP*GP*TP*TP*G)-3', ORPHAN NUCLEAR RECEPTOR NR1D1, ... (5 entities in total) |
| 機能のキーワード | orphan receptor, nuclear receptor, dna-binding, reverb, rev-erb, transcription-dna complex, transcription/dna |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| 細胞内の位置 | Nucleus (Potential): P20393 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 34333.61 |
| 構造登録者 | |
| 主引用文献 | Sierk, M.L.,Zhao, Q.,Rastinejad, F. DNA Deformability as a Recognition Feature in the RevErb Response Element Biochemistry, 40:12833-12843, 2001 Cited by PubMed Abstract: Most nuclear receptors recognize the same consensus hexameric sequence, AGGTCA. An important question has been how the various members of this transcription factor family distinguish identity features in these closely related DNA sites. We determined structures from several crystal forms of the RevErb-DNA complex and analyzed the patterns of protein-DNA interactions and DNA distortions. We found a significant and consistent DNA distortion at a TA step directly preceding the first consensus 5'-AGGTCA-3' recognition sequence. Importantly, while this base-pair sequence is associated with RevErb's high-affinity sites, there are no sequence-specific contacts formed with the protein. Our study shows that RevErb relies instead on the intrinsic geometry and flexibility of this TA site to make the required fit between the proteins' independent major groove and minor groove binding interactions, which occur on both sides of the TA step. Our findings extend the description of response element discrimination to include a role for sequence-dependent DNA deformations and suggest how other monomeric members of this superfamily, such as NGFI-B, SF-1, and ROR, could also recognize unique geometric features in their DNA targets. PubMed: 11669620DOI: 10.1021/bi011086r 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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